In biochemistry, a metalloprotein is a generic term for a protein that also contains a metalcofactor. The metal may be an isolated ion or may be coordinated with an nonprotein organic compound, such as the porphyrin found in hemoproteins. In some cases, the metal is co-coordinated with a side chain of the protein and an inorganic nonmetallic ion. This kind of protein-metal-nonmetal structure is seen in iron-sulfur clusters. Biochemistry is the chemistry of life. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... Hot metal work from a blacksmith In chemistry, a metal (Greek: Metallon) is an element that readily forms ions (cations) and has metallic bonds, and metals are sometimes described as a lattice of positive ions (cations) in a cloud of electrons. ... A cofactor is the following: In mathematics a cofactor is the minor of an element of a square matrix. ... An ion is an elementary particle or system of elementary particles with a net electric charge. ... A complex in chemistry and biochemistry is a reversible association of molecules, atoms, or ions through weak non-covalent chemical bonds. ... An organometallic compound is partially characterized by the presence of one or more metal-carbon bonds, in which the carbon involved would, apart from the metal-carbon bond, be otherwise considered a part of an organic compound. ... A porphyrin is a heterocyclic macrocycle made from 4 pyrrole subunits linked on opposite sides through 4 methine bridges. ... A hemoprotein, or heme protein, is a protein containing a heme prosthetic group, either covalently or noncovalently bound to the protein itself. ... An iron-sulfur cluster is a structural motif found in certain metalloproteins, such as the ferredoxins, as well as NADH dehydrogenase and Coenzyme Q - cytochrome c reductase of the electron transfer system. ...
The fundamental experiments on isolated metalloproteins show the complexity of measuring metal-protein association in biological samples.
In the case of putative metalloproteins the investigation of metal binding is a prerequisite for studying fundamental structure-function relationships.
Complementary determination of molar mass of the apoproteins by LC-ESI-TOF-MS was necessary as the loss of the N-terminus or point mutations occurring during heterologous expression changed the sulfur content of the protein.
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